J4 ›› 2009, Vol. 47 ›› Issue (05): 1081-1085.

• 生命科学 • 上一篇    下一篇

 重组基质金属蛋白酶MT5-MMP的表达、 纯化和复性

史秀娟, 蒋坤, 房学迅   

  1. 吉林大学 分子酶学工程教育部重点实验室, 长春 130021
  • 收稿日期:2009-01-23 出版日期:2009-09-26 发布日期:2009-11-03
  • 通讯作者: 房学迅 E-mail:fangxx@jlu.edu.cn.

Expression, Purification and Refolding of Recombinant MatrixMetalloproteinase MT5MMP

SHI Xiujuan, JIANG Kun, FANG Xuexun   

  1. Key Laboratory for Molecular Enzymology and Enzyme Engineering of the Ministry of Education,Jilin University, Changchun 130021, China
  • Received:2009-01-23 Online:2009-09-26 Published:2009-11-03
  • Contact: FANG Xuexun E-mail:fangxx@jlu.edu.cn.

摘要:

对已经构建成功并转化到大肠杆菌E.coli BL21(DE3)的基质金属蛋白酶MT5MMP的催化结构域进行诱导表达, 得到分子量为21000, 包涵体形式的重组蛋白. 通过离子交换树脂对目的蛋白进行纯化后, 用凝胶过滤树脂对纯化后的蛋白进行柱上复性, 得到了具有较高活性的重组蛋白.

关键词: 基质金属蛋白酶; 包涵体; 复性

Abstract:

The authors completed the induction expression of recombinant MT5-MMP in E.coli BL21(DE3) and harvested the protein as inclusion bodies. The molecular weight of the protein is about 21 000. In addition, we purified and refolded the recombinant protein using the chromatography method to obtain the catalytically active MT5-MMP.

Key words: matrix metalloproteinase (MMP), inclusion bodies, renaturation

中图分类号: 

  • Q55